ArticleNature chemical biology2024
The β-subunit of tryptophan synthase is a latent tyrosine synthase.
Article in Nature chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Phage-assisted continuous evolution of enzymes for noncanonical tyrosine biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A pyridoxal phosphate-dependent enzyme platform for stereoselective synthesis of γ-tertiary-nitro-noncanonical amino acids.Nature communications · 2026Article
- Promiscuity-Guided Enzyme Evolution via Substrate Multiplexed Screening.Angewandte Chemie (International ed. in English) · 2026Review
- Phage-assisted continuous evolution of enzymes for noncanonical tyrosine biosynthesis.bioRxiv : the preprint server for biology · 2026Article
- ASH: A Multi-Scale, Multi-Theory Modeling Program.Journal of computational chemistry · 2026Article
- Sequence-based generative AI design of versatile tryptophan synthases.Nature communications · 2026Article
- A pseudoenzyme enables indole biosynthesis in eudicot plants.Nature chemical biology · 2026Article
- Optimizing L-Tryptophan Production inJournal of microbiology and biotechnology · 2025Article
- Biocatalytic Synthesis of N-Protected α-Amino Acids through 1,3-Nitrogen Migration by Nonheme Iron Enzymes.Journal of the American Chemical Society · 2025Article
- Active site diversification of a non-canonical amino acid decarboxylase by merging substrate multiplexed screening with computationally guided recombination.Protein science : a publication of the Protein Society · 2025Article
- Coordinated synthesis of aromatic amino acid derived pigments in yeast via global transcriptional engineering.Microbial cell factories · 2025Article
- Designing Enzymatic Reactivity with an Expanded Palette.Chembiochem : a European journal of chemical biology · 2025Review
- Engineered Biocatalysts for the Asymmetric Synthesis of d-Phenylalanines.ACS catalysis · 2025Review
- Promiscuity Guided Evolution of Decarboxylative Aldolases for Synthesis of Tertiary γ-Hydroxy Amino Acids.Angewandte Chemie (International ed. in English) · 2025Article
- Tryptophan production by catalysis of a putative tryptophan synthase protein.Archives of microbiology · 2024Article
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7 authors.
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Abstract
Aromatic amino acids and their derivatives are diverse primary and secondary metabolites with critical roles in protein synthesis, cell structure and integrity, defense and signaling. All de novo aromatic amino acid production relies on a set of ancient and highly conserved chemistries. Here we introduce a new enzymatic transformation for L-tyrosine synthesis by demonstrating that the β-subunit of tryptophan synthase-which natively couples indole and L-serine to form L-tryptophan-can act as a latent 'tyrosine synthase'. A single substitution of a near-universally conserved catalytic residue unlocks activity toward simple phenol analogs and yields exclusive para carbon-carbon bond formation to furnish L-tyrosines. Structural and mechanistic studies show how a new active-site water molecule orients phenols for a nonnative mechanism of alkylation, with additional directed evolution resulting in a net >30,000-fold rate enhancement. This new biocatalyst can be used to efficiently prepare valuable L-tyrosine analogs at gram scales and provides the missing chemistry for a conceptually different pathway to L-tyrosine.
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